3NIP
Crystal structure of Pseudomonas aeruginosa guanidinopropionase complexed with 1,6-diaminohexane
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047972 | molecular_function | guanidinopropionase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047972 | molecular_function | guanidinopropionase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047972 | molecular_function | guanidinopropionase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047972 | molecular_function | guanidinopropionase activity |
| E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047972 | molecular_function | guanidinopropionase activity |
| F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047972 | molecular_function | guanidinopropionase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 16D B 327 |
| Chain | Residue |
| B | ARG51 |
| C | VAL298 |
| B | PRO246 |
| B | PRO250 |
| B | PRO255 |
| B | ILE257 |
| C | PHE248 |
| C | GLY292 |
| C | ALA294 |
| C | LEU297 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 16D B 328 |
| Chain | Residue |
| B | PHE248 |
| B | GLY292 |
| B | ALA294 |
| B | LEU297 |
| B | VAL298 |
| B | HOH369 |
| B | HOH830 |
| E | ARG51 |
| E | PRO246 |
| E | PRO250 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 16D D 327 |
| Chain | Residue |
| D | ARG51 |
| D | PRO246 |
| D | PRO250 |
| F | PHE248 |
| F | GLY292 |
| F | ALA294 |
| F | LEU297 |
| F | VAL298 |
| F | HOH828 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 16D D 328 |
| Chain | Residue |
| A | ARG51 |
| A | PRO246 |
| A | PRO250 |
| D | PHE248 |
| D | ALA294 |
| D | LEU297 |
| D | VAL298 |
| D | HOH350 |
| D | HOH356 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 16D E 327 |
| Chain | Residue |
| C | ARG189 |
| C | GLY190 |
| C | GLU212 |
| C | GLU256 |
| C | ILE257 |
| C | HOH831 |
| E | HIS73 |
| E | GLN266 |
| E | ARG270 |
| E | LEU297 |
| E | THR301 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SFDVDvldPafaPGtgtpeigG |
| Chain | Residue | Details |
| A | SER238-GLY259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21600989","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
